N- to C-Terminal SNARE Complex Assembly Promotes Rapid Membrane Fusion

Ajaybabu V. Pobbati(Max Planck Institute for Biophysical Chemistry), Alexander Stein(Max Planck Institute for Biophysical Chemistry), Dirk Fasshauer(Max Planck Institute for Biophysical Chemistry)
Science
August 3, 2006
Cited by 398Open Access
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Abstract

Assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) syntaxin 1, SNAP-25, and synaptobrevin 2 is thought to be the driving force for the exocytosis of synaptic vesicles. However, whereas exocytosis is triggered at a millisecond time scale, the SNARE-mediated fusion of liposomes requires hours for completion, which challenges the idea of a key role for SNAREs in the final steps of exocytosis. We found that liposome fusion was dramatically accelerated when a stabilized syntaxin/SNAP-25 acceptor complex was used. Thus, SNAREs do have the capacity to execute fusion at a speed required for neuronal secretion, demonstrating that the maintenance of acceptor complexes is a critical step in biological fusion reactions.


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